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Clonorchis sinensis MF6p/HDM (CsMF6p/HDM) induces pro-inflammatory immune response in RAW 264.7 macrophage cells via NF-κB-dependent MAPK pathways

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dc.contributor.authorKang, Jung-Mi-
dc.contributor.authorYoo, Won Gi-
dc.contributor.authorLe, Huong Giang-
dc.contributor.authorLee, Jinyoung-
dc.contributor.authorSohn, Woon-Mok-
dc.contributor.authorNa, Byoung-Kuk-
dc.date.accessioned2024-05-02T05:59:26Z-
dc.date.available2024-05-02T05:59:26Z-
dc.date.created2024-04-29-
dc.date.created2024-04-29-
dc.date.created2024-04-29-
dc.date.issued2020-01-
dc.identifier.citationParasites and Vectors, Vol.13 No.1, p. 20-
dc.identifier.issn1756-3305-
dc.identifier.urihttps://hdl.handle.net/10371/200504-
dc.description.abstractBackground MF6p/host defense molecules (HDMs) are a broad family of small proteins secreted by helminth parasites. Although the physiological role of MF6p/HDMs in trematode parasites is not fully understood, their potential biological function in maintaining heme homeostasis and modulating host immune response has been proposed. Methods A gene encoding the MF6p/HDM of Clonorchis sinensis (CsMF6p/HDM) was cloned. Recombinant CsMF6p/HDM (rCsMF6p/HDM) was expressed in Escherichia coli. The biochemical and immunological properties of rCsMF6/HDM were analyzed. CsMF6p/HDM induced pro-inflammatory response in RAW 264.7 cells was analyzed by cytokine array assay, reverse transcription polymerase chain reaction, and enzyme-linked immunosorbent assay. The structural feature of CsMF6p/HDM was analyzed by three-dimensional modeling and molecular docking simulations. Results The CsMF6p/HDM shares a high level of amino acid sequence similarity with orthologs from other trematodes and is expressed in diverse developmental stages of the parasite. The rCsMF6p/HDM bound to bacteria-derived lipopolysaccharide (LPS), without effectively neutralizing LPS-induced inflammatory response in RAW 264.7 macrophage cells. Rather, the rCsMF6p/HDM induced pro-inflammatory immune response, which is characterized by the expression of TNF-alpha and IL-6, in RAW 264.7 cells. The rCsMF6p/HDM-induced pro-inflammatory immune response was regulated by JNK and p38 MAPKs, and was effectively down-regulated via inhibition of NF-kappa B. The structural analysis of CsMF6p/HDM and the docking simulation with LPS suggested insufficient capture of LPS by CsMF6p/HDM, which suggested that rCsMF6p/HDM could not effectively neutralize LPS-induced inflammatory response in RAW 264.7 cells. Conclusions Although rCsMF6p/HDM binds to LPS, the binding affinity may not be sufficient to maintain a stable complex of rCsMF6p/HDM and LPS. Moreover, the rCsMF6p/HDM-induced pro-inflammatory response is characterized by the release of IL-6 and TNF-alpha in RAW 264.7 macrophage cells. The pro-inflammatory response induced by rCsMF6p/HDM is mediated via NF-kappa B-dependent MAPK signaling pathway. These results collectively suggest that CsMF6p/HDM mediates C. sinensis-induced inflammation cascades that eventually lead to hepatobiliary diseases.-
dc.language영어-
dc.publisherBioMed Central-
dc.titleClonorchis sinensis MF6p/HDM (CsMF6p/HDM) induces pro-inflammatory immune response in RAW 264.7 macrophage cells via NF-κB-dependent MAPK pathways-
dc.typeArticle-
dc.identifier.doi10.1186/s13071-020-3882-0-
dc.citation.journaltitleParasites and Vectors-
dc.identifier.wosid000513780600001-
dc.identifier.scopusid2-s2.0-85077785761-
dc.citation.number1-
dc.citation.startpage20-
dc.citation.volume13-
dc.description.isOpenAccessY-
dc.contributor.affiliatedAuthorYoo, Won Gi-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.subject.keywordPlusPROTEIN-STRUCTURE-
dc.subject.keywordPlusACTIVATION-
dc.subject.keywordPlusPEPTIDE-
dc.subject.keywordPlusANTIGEN-
dc.subject.keywordPlusSERVER-
dc.subject.keywordPlusALPHA-
dc.subject.keywordPlusHEME-
dc.subject.keywordAuthorClonorchis sinensis-
dc.subject.keywordAuthorMF6p-
dc.subject.keywordAuthorhost defense molecule-
dc.subject.keywordAuthorLipopolysaccharide-
dc.subject.keywordAuthorPro-inflammatory immune response-
dc.subject.keywordAuthorStructure-
dc.subject.keywordAuthorDocking-
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  • College of Veterinary Medicine
  • Department of Veterinary Medicine
Research Area Microbiology, Parasitology, Tropical Medicine

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